High affinity binding of a fungal oligopeptide elicitor to parsley plasma membranes triggers multiple defense responses

Cell. 1994 Aug 12;78(3):449-60. doi: 10.1016/0092-8674(94)90423-5.

Abstract

An oligopeptide of 13 amino acids (Pep-13) identified within a 42 kDa glycoprotein elicitor from P. mega-sperma was shown to be necessary and sufficient to stimulate a complex defense response in parsley cells comprising H+/Ca2+ influxes, K+/Cl- effluxes, an oxidative burst, defense-related gene activation, and phytoalexin formation. Binding of radiolabeled Pep-13 to parsley microsomes and protoplasts was specific, reversible, and saturable. Identical structural features of Pep-13 were found to be responsible for specific binding and initiation of all plant responses analyzed. The high affinity binding site recognizing the peptide ligand (KD = 2.4 nM) may therefore represent a novel class of receptors in plants, and the rapidly induced ion fluxes may constitute elements of the signal transduction cascade triggering pathogen defense in plants.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Cell Membrane / metabolism*
  • Cells, Cultured
  • Glycoproteins / metabolism*
  • Ions
  • Microsomes / metabolism
  • Models, Biological
  • Molecular Sequence Data
  • Oligopeptides / pharmacology*
  • Phytophthora / chemistry*
  • Plant Extracts / biosynthesis
  • Protein Binding
  • Protoplasts / metabolism
  • Respiratory Burst
  • Sesquiterpenes
  • Signal Transduction*
  • Structure-Activity Relationship
  • Terpenes
  • Transcription, Genetic
  • Vegetables / microbiology
  • Vegetables / physiology*

Substances

  • Glycoproteins
  • Ions
  • Oligopeptides
  • Plant Extracts
  • Sesquiterpenes
  • Terpenes
  • phytoalexins